Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.3.1 (Mg2+-ATPase)
 1,484 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The specific activity of markers-enzymes in the subcellular fractions of the rabbit visual analyzer cortical end, the synaptosomes and mitochondria of nerve cells, changed under the effect of early long deprivation. For cytochromoxidase and Na+, K+-ATPase it lowers considerably in all subfractions, for monoaminoxidase and Mg2+-ATPase it rises mainly in synaptosomes; the activity of acetyl cholinesterase lowers per 1 g of tissue. In the light two weeks later a tendency is observed to normalization of the studied indexes. The specific activity of cytochrome oxidase (except for free mitochondria) and Na+, K+-ATPase reaches the control, that of monoaminoxidase also partially normalizes, but not competely; Mg2+ATPase in all the subfractions is more inhibited than in the control. This evidences for the effect of light deprivation on the activity of the enzymes associated with different cycles of metabolic processes, first of all, of oxidation and ion transport. These changes are reversible when visual impulsation is recovered. Disturbances in chemism at the subcellular level are specific for different enzymic systems and are not the same in certain subfractions of great hemispheres.
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PMID:[Effect of light deprivation on enzymic activity of synaptosomes and mitochondria of rabbit cortex visual region]. 19 70

Acetylcholinesterase (AchE: EC 3.1.1.7) was identified and purified from the hemolymph of the scorpion Heterometrus bengalensis. The purity of the enzyme was determined by polyacrylamide gel electrophoresis (PAGE). The molecular weight of the enzyme, determined by sodium dodecyl sulfate-PAGE, was 80,000. The purified AchE hydrolysed acetylthiocholine iodide, but it did not react with butyrylthiocholine iodide. BW284C51, a specific inhibitor of AchE, strongly inhibited the enzyme. The known inhibitor (tetramonoisopropylpyrophosphortetramide) of pseudocholinesterase did not produce any inhibition of the enzyme activity. The purified AchE of scorpion hemolymph was vulnerable to high substrate concentration. The presence of Cu2+ and Ni2+ reduced the enzyme activity, whereas the metal ion, Sn2+, enhanced AchE activity. Ca2+ produced neither inhibition nor activation. (Na+, K+)-ATPase and Mg2+-ATPase activities were greatly enhanced by the purified AchE.
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PMID:Acetylcholinesterase (EC 3.1.1.7), a neurotransmitter enzyme in scorpion hemolymph. 296 37

Human erythrocyte acetylcholinesterase and the plasma cholinesterase variants are not only inhibited by propranolol but have been found to show stereospecificity for its isomers. The erythrocyte enzyme has a greater affinity for the L-isomer than either the racemate or the D-isomer. In contrast the plasma cholinesterases have greater specificity for the D-isomer than the other isomer or racemate. The usual enzyme shows greater stereospecificity than the atypical enzyme and these findings present additional evidence that these enzyme variants differ in structure at the catalytic active site. Neither Na+ + K+ -ATPase nor Mg2+-ATPase show stereo-specificity for the isomers of propranolol although both enzymes are inhibited by the drug. The action of the drug on the four enzymes in blood samples obtained from patients having Huntington's disease was found to be identical to those observed on the enzymes in blood samples from healthy controls.
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PMID:Studies on the inhibition by propranolol of some human erythrocyte membrane enzymes and plasma cholinesterase. 612 Jul 72

Acute intraperitoneal administration of lanthanum chloride to newborn chicks at the single dose of 250 mg/kg body weight inhibits calcium binding to brain synaptosomal membrane. There is also marked depression in the activities of neural Ca2+-ATPase, Mg2+-ATPase, and cholinesterase after acute lanthanum chloride intoxication. The inhibition of these enzymes in relation to depletion of calcium binding to the synaptosomal membrane has been discussed.
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PMID:Neurotoxicity of lanthanum chloride in newborn chicks. 613 Jun 44

The widely used atrazine has been reported to exhibit extensive ecological hazards. Due to the biological accumulation, atrazine elicits widespread toxic effects on different organisms. However, true proof for the mechanism of atrazine-induced toxicity is lacking. To determine the potential mechanism by which atrazine exerted toxic effects, quails were treated with atrazine (0, 50, 250 and 500 mg/kg) by gavage administration for 45 days. Atrazine significantly increased the histological alterations and serum creatine kinase, lactate dehydrogenase and choline esterase levels. A marked disorder in ionic (Na+, K+, Ca2+ and Mg2+)contents and the decrease of ATPases (Na+-K+-ATPase, Ca2+-ATPase, Mg2+-ATPase and Ca2+-Mg2+-ATPase) activities were observed in the heart and liver of atrazine-exposed quails. Of note, it was also observed that atrazine suppressed the transcription of Na+, K+ transfer associated genes (Na+-K+-ATPase subunits) and Ca2+ transfer associated genes (Ca2+-ATPase subunits, solute carriers) in heart and liver. In conclusion, atrazine induced cardiac and hepatic damage via causing the ionic disorder, triggering the transcription of the ion transporters and leading the histopathological and functional alternations in the heart and liver of quails. This study demonstrated atrazine significantly induced the ionic disorder via decreasing the ATPases activities and disturbing the transcription of the ion transporters.
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PMID:A novel mechanism underlies atrazine toxicity in quails (Coturnix Coturnix coturnix): triggering ionic disorder via disruption of ATPases. 2792 60